Journal
EMBO JOURNAL
Volume 25, Issue 21, Pages 5094-5104Publisher
WILEY
DOI: 10.1038/sj.emboj.7601389
Keywords
CRM1; HDACs; nuclear export; protein arginine methylation; RIP140
Categories
Funding
- NCI NIH HHS [CA 90089] Funding Source: Medline
- NIDA NIH HHS [P50 DA011806, DA11190, R01 DA011190, K02-DA13926, DA11806, K02 DA013926] Funding Source: Medline
- NIDDK NIH HHS [R01 DK060521, DK54733, DK60521, R01 DK054733] Funding Source: Medline
Ask authors/readers for more resources
Receptor interacting protein 140 (RIP140), a ligand-dependent corepressor for nuclear receptors, can be modified by arginine methylation. Three methylated arginine residues, at Arg-240, Arg-650, and Arg-948, were identified by mass spectrometric analysis. Site-directed mutagenesis studies demonstrated the functionality of these arginine residues. The biological activity of RIP140 was suppressed by protein arginine methyltransferase 1 (PRMT1) due to RIP140 methylation, which reduced the recruitment of histone deacetylases to RIP140 and facilitated its nuclear export by enhancing interaction with exportin 1. A constitutive negative (Arg/Ala) mutant of RIP140 was resistant to the effect of PRMT1, and a constitutive positive (Arg/Phe) mutation mimicked the effect of arginine methylation. The biological activities of the wild type and the mutant proteins were examined in RIP140-null MEF cells. This study uncovered a novel means to inactivate, or suppress, RIP140, and demonstrated protein arginine methylation as a critical type of modification for corepressor.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available